Arylformamidase: Difference between revisions
Thomasparker (talk | contribs) |
Thomasparker (talk | contribs) |
||
| Line 5: | Line 5: | ||
== Abstract == | == Abstract == | ||
2PBL, initially annotated as an arylformamidase, was isolated from ''Silicibacter sp. TM1040'' and its structure determined by the JCSG. Based on structural, functional and evolutionary analysis, we have further characterised 2PBL. It was found to contain conserved functional | 2PBL, initially annotated as an arylformamidase, was isolated from ''Silicibacter sp. TM1040'' and its structure determined by the JCSG. Based on structural, functional and evolutionary analysis, we have further characterised 2PBL. It was found to contain a conserved functional region present in A/B-hydrolases of many taxonomic groups. Specifically, it was found to share similar structural and sequence characteristics of the prokaryotic HSL family of esterases. Residues of a probable catalytic triad were identified as Ser137, His242 and Glu215. Further experimental characterisation of 2PBL is required to better understand its function. | ||
== Contents == | == Contents == | ||
Revision as of 01:23, 10 June 2008
by Basma Al Alaiwat, Sebastian Mynott and Thomas Parker
Abstract
2PBL, initially annotated as an arylformamidase, was isolated from Silicibacter sp. TM1040 and its structure determined by the JCSG. Based on structural, functional and evolutionary analysis, we have further characterised 2PBL. It was found to contain a conserved functional region present in A/B-hydrolases of many taxonomic groups. Specifically, it was found to share similar structural and sequence characteristics of the prokaryotic HSL family of esterases. Residues of a probable catalytic triad were identified as Ser137, His242 and Glu215. Further experimental characterisation of 2PBL is required to better understand its function.
Contents
Presentations
Sequence & Homology - Sebastian Mynott
Structure - Basma Al Alaiwat
Function - Thomas Parker
